Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5506
pubmed:dateCreated
2001-2-22
pubmed:abstractText
We cloned and characterized a protein kinase and ion channel, TRP-PLIK. As part of the long transient receptor potential channel subfamily implicated in control of cell division, it is a protein that is both an ion channel and a protein kinase. TRP-PLIK phosphorylated itself, displayed a wide tissue distribution, and, when expressed in CHO-K1 cells, constituted a nonselective, calcium-permeant, 105-picosiemen, steeply outwardly rectifying conductance. The zinc finger containing alpha-kinase domain was functional. Inactivation of the kinase activity by site-directed mutagenesis and the channel's dependence on intracellular adenosine triphosphate (ATP) demonstrated that the channel's kinase activity is essential for channel function.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0036-8075
pubmed:author
pubmed:issnType
Print
pubmed:day
9
pubmed:volume
291
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1043-7
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:11161216-Adenosine Triphosphate, pubmed-meshheading:11161216-Amino Acid Motifs, pubmed-meshheading:11161216-Amino Acid Sequence, pubmed-meshheading:11161216-Animals, pubmed-meshheading:11161216-CHO Cells, pubmed-meshheading:11161216-Calcium, pubmed-meshheading:11161216-Catalytic Domain, pubmed-meshheading:11161216-Cations, pubmed-meshheading:11161216-Cell Line, pubmed-meshheading:11161216-Cricetinae, pubmed-meshheading:11161216-DNA, Complementary, pubmed-meshheading:11161216-Electric Conductivity, pubmed-meshheading:11161216-Humans, pubmed-meshheading:11161216-Ion Channels, pubmed-meshheading:11161216-Membrane Proteins, pubmed-meshheading:11161216-Mice, pubmed-meshheading:11161216-Molecular Sequence Data, pubmed-meshheading:11161216-Mutation, pubmed-meshheading:11161216-Myelin Basic Proteins, pubmed-meshheading:11161216-Patch-Clamp Techniques, pubmed-meshheading:11161216-Phosphorylation, pubmed-meshheading:11161216-Protein Kinases, pubmed-meshheading:11161216-Rats, pubmed-meshheading:11161216-Recombinant Fusion Proteins, pubmed-meshheading:11161216-TRPM Cation Channels, pubmed-meshheading:11161216-Transfection, pubmed-meshheading:11161216-Two-Hybrid System Techniques, pubmed-meshheading:11161216-Type C Phospholipases
pubmed:year
2001
pubmed:articleTitle
TRP-PLIK, a bifunctional protein with kinase and ion channel activities.
pubmed:affiliation
Howard Hughes Medical Institute, Department of Cardiology, Department of Neurobiology, Harvard Medical School, 1309 Enders Building, 320 Longwood Avenue, Children's Hospital, Boston, MA 02115, USA.
pubmed:publicationType
Journal Article